Reviewed, UniProtKB/Swiss-Prot O42227 (HDA1B_XENLA)

Names and origin

Protein names

Recommended name:
    Probable histone deacetylase 1-B
      Short name=HD1
    EC=3.5.1.98
Alternative name(s):
    RPD3 homolog

Gene names

Name:

hdac1-B

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Ref.3
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Found in a large complex with RBBP4 and MI-2.
Subcellular location	Cytoplasm. Nucleus. Ref.3
Sequence similarities	Belongs to the histone deacetylase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
Gene Ontology (GO)
Biological process	histone deacetylation Inferred from electronic annotation. Source: InterPro regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone deacetylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 480	480	Probable histone deacetylase 1-B		PRO_0000114692
Regions
	Region	10 – 321	312	Histone deacetylase
	Compositional bias	299 – 302	4	Poly-Gly
Sites
	Active site	141	1	By similarity
Experimental info
	Mutagenesis	141	1	H → A: Abolishes histone deacetylase activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O42227-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: CA92DE34D36E39E8	FASTA	480	54,893
	10 20 30 40 50 60 MALSQGTKKK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAS 70 80 90 100 110 120 AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS 130 140 150 160 170 180 AVKLNKQQTD ISVNWSGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV VYIDIDIHHG 190 200 210 220 230 240 DGVEEAFYTT DRVMSVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI 250 260 270 280 290 300 FKPVMTKVME MFQPSAVVLQ CGADSLSGDR LGCFNLTIKG HAKCVEFIKT FNLPMLMLGG 310 320 330 340 350 360 GGYTIRNVAR CWTYETAVAL DSEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE 370 380 390 400 410 420 KIKQRLFENL RMLPHAPGVQ MQAIPEDSVH DDSGEEDEED PDKRISIRSS DKRIACDEEF 430 440 450 460 470 480 SDSEDEGEGG RKNVANFKKV KRVKTEEEKE GEDKKDVKEE EKAKDEKTDS KRVKEETKSV

References

[1]	"Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase." Wong J., Patterton D., Imhof A., Guschin D., Shi Y.-B., Wolffe A.P. EMBO J. 17:520-534(1998) [PubMed: 9430643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A multiple subunit Mi-2 histone deacetylase from Xenopus laevis cofractionates with an associated Snf2 superfamily ATPase." Wade P.A., Jones P.L., Vermaak D., Wolffe A.P. Curr. Biol. 8:843-846(1998) [PubMed: 9663395] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH RBBP4 AND MI-2.
[3]	"Functional analysis of the SIN3-histone deacetylase RPD3-RbAp48-histone H4 connection in the Xenopus oocyte." Vermaak D., Wade P.A., Jones P.L., Shi Y.-B., Wolffe A.P. Mol. Cell. Biol. 19:5847-5860(1999) [PubMed: 10454532] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RBBP4, MUTAGENESIS OF HIS-141.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF020658 mRNA. Translation: AAC60346.1.
3D structure databases
HSSP	HSSP built from PDB template 1C3P based on UniProtKB O67135.
ModBase	Search...
Phylogenomic databases
HOVERGEN	O42227.
Family and domain databases
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHER	PTHR10625. His_deacetylse. 1 hit. PTHR10625:SF28. His_deacetylse_1. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProtoNet	Search...

Entry information

Entry name

HDA1B_XENLA

Accession

Primary (citable) accession number: O42227

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	September 22, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project